ID A0A1D1VWJ2_RAMVA Unreviewed; 1989 AA.
AC A0A1D1VWJ2;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:GAV05830.1};
GN Name=RvY_15901-1 {ECO:0000313|EMBL:GAV05830.1};
GN Synonyms=RvY_15901.1 {ECO:0000313|EMBL:GAV05830.1};
GN ORFNames=RvY_15901 {ECO:0000313|EMBL:GAV05830.1};
OS Ramazzottius varieornatus (Water bear) (Tardigrade).
OC Eukaryota; Metazoa; Ecdysozoa; Tardigrada; Eutardigrada; Parachela;
OC Hypsibioidea; Ramazzottiidae; Ramazzottius.
OX NCBI_TaxID=947166 {ECO:0000313|EMBL:GAV05830.1, ECO:0000313|Proteomes:UP000186922};
RN [1] {ECO:0000313|EMBL:GAV05830.1, ECO:0000313|Proteomes:UP000186922}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YOKOZUNA-1 {ECO:0000313|EMBL:GAV05830.1,
RC ECO:0000313|Proteomes:UP000186922};
RX PubMed=27649274; DOI=10.1038/ncomms12808;
RA Hashimoto T., Horikawa D.D., Saito Y., Kuwahara H., Kozuka-Hata H.,
RA Shin-I T., Minakuchi Y., Ohishi K., Motoyama A., Aizu T., Enomoto A.,
RA Kondo K., Tanaka S., Hara Y., Koshikawa S., Sagara H., Miura T.,
RA Yokobori S., Miyagawa K., Suzuki Y., Kubo T., Oyama M., Kohara Y.,
RA Fujiyama A., Arakawa K., Katayama T., Toyoda A., Kunieda T.;
RT "Extremotolerant tardigrade genome and improved radiotolerance of human
RT cultured cells by tardigrade-unique protein.";
RL Nat. Commun. 7:12808-12808(2016).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004606}; Single-
CC pass type II membrane protein {ECO:0000256|ARBA:ARBA00004606}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00196}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GAV05830.1}.
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DR EMBL; BDGG01000012; GAV05830.1; -; Genomic_DNA.
DR STRING; 947166.A0A1D1VWJ2; -.
DR Proteomes; UP000186922; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd00112; LDLa; 8.
DR Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 8.
DR Gene3D; 3.30.70.960; SEA domain; 1.
DR Gene3D; 3.10.250.10; SRCR-like domain; 1.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 3.
DR InterPro; IPR036055; LDL_receptor-like_sf.
DR InterPro; IPR023415; LDLR_class-A_CS.
DR InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR000082; SEA_dom.
DR InterPro; IPR036364; SEA_dom_sf.
DR InterPro; IPR001190; SRCR.
DR InterPro; IPR017448; SRCR-like_dom.
DR InterPro; IPR036772; SRCR-like_dom_sf.
DR InterPro; IPR001254; Trypsin_dom.
DR PANTHER; PTHR24270:SF61; CD320 ANTIGEN; 1.
DR PANTHER; PTHR24270; LOW-DENSITY LIPOPROTEIN RECEPTOR-RELATED; 1.
DR Pfam; PF00057; Ldl_recept_a; 6.
DR Pfam; PF01390; SEA; 1.
DR Pfam; PF15494; SRCR_2; 1.
DR Pfam; PF00089; Trypsin; 2.
DR PRINTS; PR00261; LDLRECEPTOR.
DR SMART; SM00192; LDLa; 9.
DR SMART; SM00202; SR; 1.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF57424; LDL receptor-like module; 7.
DR SUPFAM; SSF82671; SEA domain; 1.
DR SUPFAM; SSF56487; SRCR-like; 2.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 2.
DR PROSITE; PS01209; LDLRA_1; 2.
DR PROSITE; PS50068; LDLRA_2; 7.
DR PROSITE; PS50024; SEA; 1.
DR PROSITE; PS50287; SRCR_2; 2.
DR PROSITE; PS50240; TRYPSIN_DOM; 2.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00196}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000186922};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825};
KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 174..200
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 299..414
FT /note="SEA"
FT /evidence="ECO:0000259|PROSITE:PS50024"
FT DOMAIN 976..1085
FT /note="SRCR"
FT /evidence="ECO:0000259|PROSITE:PS50287"
FT DOMAIN 1120..1308
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT DOMAIN 1620..1719
FT /note="SRCR"
FT /evidence="ECO:0000259|PROSITE:PS50287"
FT DOMAIN 1763..1983
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT REGION 111..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 715..736
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1320..1383
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 111..134
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 720..734
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1356..1371
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 807..822
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 847..862
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 935..950
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 960..978
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1023..1084
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 1514..1532
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1553..1571
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1604..1619
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1709..1719
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
SQ SEQUENCE 1989 AA; 215647 MW; C0642E95DEE623DD CRC64;
MLKFHPAAKM KDKPIVPTSI VTSLKPDGTV MNPAFQTVDI DGLSSQINGS TYGSYHTLSN
DNYPTRSVST VSPVSKTDVP GGQLNHTFLR EATDPNANVY PEREAHYFGK SLPRVEKDPS
AGHDGSRRSY SPTEDRELPT YYMPVNAHRK LLRGEILYVT KDTRKSKSKC WKRTLCIALI
AAVLIIAVVI GSLSAVGIIF NPRNVEQRKD NLQALSVTSD GLRSAVDIEV QEIDKRVETS
PSRLHPGSER EPKLISNSAG GINGVSEQAG HGRLPVDGSV TGTTQSTLEL FQIGPVEGVP
EAVEGELRIL NMDFQMALAD HKSWLYQYTA NDLATYLTDI FIKAVNAENF NATRVISFRP
GSVIAKFQAL WNQAPANWDA VVTQVMNNHL DLNSNFIGNY LIDRGSLSIK SIFYTCRVDN
GGCSHLCEFD LLEMKQYCLC PDNRYTLMNL TTCALTSGLS AVTTRTTPVT PSMTVPPLRP
TETTIYTSLI TSRALFTVEN LNTTVSPGRN SDPSFLHLVP VNTAEVPREP GVVTGPSTMN
HSSDHNAALV HYSIEESTTI TTAVSAQQNT TSSTPSIGTT GGQGSTTLSP LSRYSTWWTV
LSLLNQQQST TSPSTTTSTT TVGVITLETT TEVLPLIERT GLTEDFPAHL LSSTPLPGLS
HEAGGGHLDV HSVSTAMNTT NVTSEVGEPA VQSQISHENE TFVGHVPPAL IASTEPVEGS
TTEHNEDVLE SEDGHGTSTR ALVETTMSTS GAVEHDVTEA PHHAMPSPDP NFVTLLHPVH
PINSSACTSD QFHCVSEDRC ISSLARCNGV SECEDRSDEN ECLDCGQNFR CSKEPGLSEC
IPVGLVCDGL QDCQNGRDEQ SCTQNFCQAS GMFQCVTGYC LENSSRCDGM GDCYAMGVPI
DELNCLNSEQ SYQCADAGHF MCTESRRCIP MEWRCNKRTD CLDDEDEKAC SCPSGLTFAC
DGGGCINSHY RCDGVAQCAD GYSDEVGCTR LEPSGLLEVQ SDANDWFPVC SDNWVKNSAD
AVCSRLGYRP ALSVFSLAAE VTNHSEFFWS SREFNATSPI QGQLRVFSTA GRCQNGNARA
GVTCERFRCQ LNANPADEAP AKLLSSIVKI TFEGDPFIAC NGYLVAPMWI VTSASCLTNR
TAPLLRVAFQ DQTIQAGVIE VLQHPQYVPI RMMHDRDFAL LRLSNSVPAS VLPHCLPSEN
VLPRQCKLIR LHTNGSFSSH DLTSLPITEC NEKNVYANLI SGSMECWTVN VSVCDEDAVS
PMLCETTEGG WELRGFLSYQ HHCGFFYKKP LVMSNLTFAA KWMRSVVGPS LTNVVRDVPP
AAATTPSSEL SSSSEASHAE EHHESAAVDA HQPPPVGSHE PVPPPEPHQA PAAPAAHGAE
HNLHGDADSI SERAQINSKK ALVMFGAPRV LQESNTTSIP AVLNVSFVSN ISATLFDNVT
TKAVTAAEAP LLTTIVSTPS TSTVPSVPFL TCPNGVLLLP EYLCDGIENC GDGWDENVAN
CMAMPCDQPT HQRCAGGRCV EAIAVCDGRS QCPINSTDEI GCKECDTTTH FRCLEGRCVS
LSWMDDGVPD CLNGEDEASV GSCNSTTSYR CVYGGGCIPN EKVCDGVSDC PSNSDESDCV
RVYHSYDTPS GVVGMRSRGS VWTPICHSGH STGAEKQWGE KVCRELGYDF SNATNPEFSA
NITGFTISDH APAEVDIYMT ERNLTAGRCN NSEILAASCG SVERGNWNSN VTALDLAVAY
RVPREEYRHI ALLIHVKGAL EPCIGTFLNA RWLITSYECL TEVDSSLAPF DWVISTDPNS
VTDDSLRFVR RFVAHPNAKF RVYFAQHDLV LVELMEDVNL TGGISKAGLV PISGPLPDST
CVTYGWLYDT VEIPGTKVQR KSQGRLYSWR TPLVPTAQCN QAGNYNGLVD ASSQFCGGFR
NATHRSPCMG RIDGAPVMCL NAGDRWEITG VRAFQPNCES SWVAPSVYTD VFQHRKWLGD
IVGSGLLDK
//
